CPN1

Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene.

CPN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2NSM
Identifiers
Aliases	CPN1, CPN, SCPN, carboxypeptidase N subunit 1
External IDs	OMIM: 603103; MGI: 2135874; HomoloGene: 1002; GeneCards: CPN1; OMA:CPN1 - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10q24.2 Start 100,042,193 bp End 100,081,869 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19 C3|19 36.68 cM Start 43,944,746 bp End 43,974,995 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver gonad testicle buccal mucosa cell mucosa of ileum skin of thigh right testis left testis kidney human kidney Top expressed in left lobe of liver yolk sac islet of Langerhans epithelium of stomach blastocyst right kidney pyloric antrum proximal tubule morula morula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function carboxypeptidase activity peptidase activity zinc ion binding hydrolase activity metallopeptidase activity metal ion binding metallocarboxypeptidase activity serine-type carboxypeptidase activity Cellular component extracellular space Golgi apparatus secretory granule soma synaptic membrane extracellular region Biological process response to glucocorticoid bradykinin catabolic process proteolysis insulin processing regulation of complement activation peptide metabolic process protein processing Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1369 93721 Ensembl ENSG00000120054 ENSMUSG00000025196 UniProt P15169 Q9JJN5 RefSeq (mRNA) NM_001308 NM_030703 RefSeq (protein) NP_001299 NP_109628 Location (UCSC) Chr 10: 100.04 – 100.08 Mb Chr 19: 43.94 – 43.97 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer composed of two identical regulatory subunits and two identical catalytic subunits; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency.

In melanocytic cells CPN1 gene expression may be regulated by MITF.

External links

• Human CPN1 genome location and CPN1 gene details page in the UCSC Genome Browser.

Further reading

• Matthews KW, Mueller-Ortiz SL, Wetsel RA (2004). "Carboxypeptidase N: a pleiotropic regulator of inflammation". Mol. Immunol. 40 (11): 785–93. doi:10.1016/j.molimm.2003.10.002. PMID 14687935.
• Gebhard W, Schube M, Eulitz M (1990). "CDNA Cloning of Kininase 1". Kinins V. Advances in Experimental Medicine and Biology. Vol. 247B. pp. 261–4. doi:10.1007/978-1-4615-9546-5_43 (inactive 2024-11-02). ISBN 978-1-4615-9548-9. PMID 2610070.{{cite book}}: CS1 maint: DOI inactive as of November 2024 (link)
• Skidgel RA, Bennett CD, Schilling JW, et al. (1988). "Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: comparison with other carboxypeptidases". Biochem. Biophys. Res. Commun. 154 (3): 1323–9. doi:10.1016/0006-291X(88)90284-7. PMID 3408501.
• Hendriks D, Vingron M, Vriend G, et al. (1994). "On the specificity of carboxypeptidase N, a comparative study". Biol. Chem. Hoppe-Seyler. 374 (9): 843–9. doi:10.1515/bchm3.1993.374.7-12.843. PMID 8267877.
• Sato T, Miwa T, Akatsu H, et al. (2000). "Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not". J. Immunol. 165 (2): 1053–8. doi:10.4049/jimmunol.165.2.1053. PMID 10878383.
• Campbell WD, Lazoura E, Okada N, Okada H (2002). "Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N." Microbiol. Immunol. 46 (2): 131–4. doi:10.1111/j.1348-0421.2002.tb02669.x. PMID 11939578. S2CID 33755040.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Cao H, Hegele RA (2003). "DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency". J. Hum. Genet. 48 (1): 20–2. doi:10.1007/s100380300003. PMID 12560874.
• Shimomura Y, Kawamura T, Komura H, et al. (2003). "Modulation of procarboxypeptidase R (ProCPR) activation by complementary peptides to thrombomodulin". Microbiol. Immunol. 47 (3): 241–5. doi:10.1111/j.1348-0421.2003.tb03383.x. PMID 12725295. S2CID 24243086.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Davis DA, Singer KE, De La Luz Sierra M, et al. (2005). "Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation". Blood. 105 (12): 4561–8. doi:10.1182/blood-2004-12-4618. PMC 1895000. PMID 15718415.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.